BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 15661

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15661
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Solution NMR Structure of protein hp1203 from Helicobacter pylori 26695

Deposition date: 2008-02-18 Original release date: 2009-05-07

Authors: Wu, Bin; Yee, Adelinda; Lemak, Alexander; Cort, John; Semest, Anthony; Kenney, Michael; Arrowsmith, Cheryl

Citation: Wu, Bin; Yee, Adelinda; Lemak, Alexander; Cort, John; Semest, Anthony; Kenney, Michael; Arrowsmith, Cheryl. "Solution NMR structure of protein hp1203 from helicobacter pyloric 26695/Northeast Structure Genomics Consortium (NESG) target PT1/Ontario Center for Structural Proteomics target hp1203"  . ., .-..

Assembly members:
hp1203, polymer, 110 residues, 25879.195 Da.

Natural source:   Common Name: not available   Taxonomy ID: 210   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Helicobacter pylori

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
hp1203: MLEDYAISLEEVNFNDFIVV DVRELDEYEELHLPNATLIS VNDQEKLADFLSQHKDKKVL LHCRAGRRALDAAKSMHELG YTPYYLEGNVYDFEKYGFRM VYDDTCDKKN

Data sets:
Data typeCount
13C chemical shifts479
15N chemical shifts119
1H chemical shifts795

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1unknown_function_protein_hp1203_from_Helicobacter_pylori_266951

Entities:

Entity 1, unknown_function_protein_hp1203_from_Helicobacter_pylori_26695 110 residues - 25879.195 Da.

1   METLEUGLUASPTYRALAILESERLEUGLU
2   GLUVALASNPHEASNASPPHEILEVALVAL
3   ASPVALARGGLULEUASPGLUTYRGLUGLU
4   LEUHISLEUPROASNALATHRLEUILESER
5   VALASNASPGLNGLULYSLEUALAASPPHE
6   LEUSERGLNHISLYSASPLYSLYSVALLEU
7   LEUHISCYSARGALAGLYARGARGALALEU
8   ASPALAALALYSSERMETHISGLULEUGLY
9   TYRTHRPROTYRTYRLEUGLUGLYASNVAL
10   TYRASPPHEGLULYSTYRGLYPHEARGMET
11   VALTYRASPASPTHRCYSASPLYSLYSASN

Samples:

sample_1: unknown function protein hp1203 from Helicobacter pylori 26695, [U-99% 13C; U-99% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 10 mM; H2O 90%; D2O 10%

sample_2: unknown function protein hp1203 from Helicobacter pylori 26695, [U-7% 13C; U-99% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 10 mM; H2O 90%; D2O 10%

sample_conditions_2: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
aiv 3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_2

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.95, Goddard - data analysis, peak picking

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.0, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct v2.1.0, Huang, Tejero, Powers and Montelione - Validation

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAJ56270 BAJ58734 BAJ60256 BAO97236
EMBL CAX29900 CBI65819
GB AAD08279 ABF85232 ACI27917 ACX99708 ADN80346
REF NP_208015 WP_000888636 WP_000888781 WP_000888783 WP_000888785

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts